PACC_YARLI
ID PACC_YARLI Reviewed; 585 AA.
AC P78978; Q6CER5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=pH-response transcription factor pacC/RIM101;
GN Name=RIM101; Synonyms=RPH2; OrderedLocusNames=YALI0B13640g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
RP 331-VAL--CYS-585; 420-GLN--CYS-585 AND 474-LEU--CYS-585.
RX PubMed=9199331; DOI=10.1128/mcb.17.7.3966;
RA Lambert M., Blanchin-Roland S., Le Louedec F., Lepingle A., Gaillardin C.;
RT "Genetic analysis of regulatory mutants affecting synthesis of
RT extracellular proteinases in the yeast Yarrowia lipolytica: identification
RT of a RIM101/pacC homolog.";
RL Mol. Cell. Biol. 17:3966-3976(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [3]
RP DNA-BINDING.
RX PubMed=10206713; DOI=10.1099/13500872-145-1-75;
RA Madzak C., Blanchin-Roland S., Cordero-Otero R.R., Gaillardin C.;
RT "Functional analysis of upstream regulating regions from the Yarrowia
RT lipolytica XPR2 promoter.";
RL Microbiology 145:75-87(1999).
RN [4]
RP FUNCTION.
RX PubMed=11861549; DOI=10.1093/genetics/160.2.417;
RA Gonzalez-Lopez C.I., Szabo R., Blanchin-Roland S., Gaillardin C.;
RT "Genetic control of extracellular protease synthesis in the yeast Yarrowia
RT lipolytica.";
RL Genetics 160:417-427(2002).
CC -!- FUNCTION: Transcription factor that mediates regulation of both
CC acid- and alkaline-expressed genes in response to ambient pH. At
CC alkaline ambient pH, activates transcription of alkaline-expressed
CC genes (including RIM101 itself) and represses transcription of acid-
CC expressed genes, thereby regulating the synthesis and secretion of
CC alkaline protease XPR2 and acidic protease AXP1 depending on ambient
CC pH. Specifically recognizes and binds the consensus sequence 5'-GCCARG-
CC 3'. Required for mating and sporulation. {ECO:0000269|PubMed:11861549,
CC ECO:0000269|PubMed:9199331}.
CC -!- SUBUNIT: Binds to DNA. Interacts with RIM20, which binds to the two
CC YPX[LI] motifs and is required for proteolytic processing (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Activated by C-terminal proteolytic cleavage by signaling protease
CC (probably palB/RIM13) at neutral to alkaline ambient pH. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pacC/RIM101 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X99616; CAA67927.1; -; Genomic_DNA.
DR EMBL; CR382128; CAG83098.1; -; Genomic_DNA.
DR RefSeq; XP_500847.1; XM_500847.1.
DR AlphaFoldDB; P78978; -.
DR STRING; 4952.CAG83098; -.
DR EnsemblFungi; CAG83098; CAG83098; YALI0_B13640g.
DR GeneID; 2907295; -.
DR KEGG; yli:YALI0B13640g; -.
DR VEuPathDB; FungiDB:YALI0_B13640g; -.
DR HOGENOM; CLU_466307_0_0_1; -.
DR InParanoid; P78978; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..585
FT /note="pH-response transcription factor pacC/RIM101"
FT /id="PRO_0000046846"
FT ZN_FING 146..171
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 182..206
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 212..234
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 471..474
FT /note="YPX[LI] motif 1"
FT MOTIF 579..582
FT /note="YPX[LI] motif 2"
FT COMPBIAS 84..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 331..585
FT /note="Missing: In RIM101-1119; dominant active allele that
FT activates XPR2 transcription independent on ambient pH."
FT /evidence="ECO:0000269|PubMed:9199331"
FT MUTAGEN 420..585
FT /note="Missing: In RIM101-5; dominant active allele that
FT activates XPR2 transcription independent on ambient pH."
FT /evidence="ECO:0000269|PubMed:9199331"
FT MUTAGEN 474..585
FT /note="Missing: In RIM101-1116; dominant active allele that
FT activates XPR2 transcription independent on ambient pH."
FT /evidence="ECO:0000269|PubMed:9199331"
SQ SEQUENCE 585 AA; 64326 MW; E6B10AEAC00C2B51 CRC64;
MASYPYLAQS QPPQQQQQQQ QQPQQQSQQL PTTAPSAAPQ VNNTTANKPL YPASPNSPIS
PSDYSANMNV GGDSVDMLLS SVSAHHRSSD AGQSDMGSIS PSTAHTTPDA TTYKTSDEED
ATGKITTPRS EGSPNTNGSG SDGENLVCKW GPCGKTFGSA EKLYAHLCDA HVGRKCTHNL
SLVCNWDNCG IVTVKRDHIT SHIRVHVPLK PYKCDFCTKS FKRPQDLKKH VKTHADDNEQ
AHNAYAKPHM QHTHQQQQQQ QRYMQYPTYA SGYEYPYYRY SQPQVQVPMV PSYAAVGHMP
TPPMHPHAPI DRKRQWDTTS DFFDDIKRAR VTPNYSSDIA SRLSTIEQYI GIQGQQQQAS
PTPQTATTTS ATPAPAAPHQ ATPPQQQLPS FKQGDYQETD QFLNQLGSNI YGNIKSVDPQ
YEAPAEFHLP HPMGYRYAFS HAPAPHGAAP VAPQVAPPAH PGVHGVSAPH YPDLSYSRST
VPQLSSRFED VRQMSVGVTQ RAARTTNVEE SDDDDELVEG FGKMAIADSK AMQVAQMKKH
LEVVSYLRRV LQEARETESG EAEDTAANKD TSASKSSLYP TIKAC
